PDBe 2h48

X-ray diffraction
2.2Å resolution

Crystal structure of human caspase-1 (Cys362->Ala, Cys364->Ala, Cys397->Ala) in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK)

Released:
Source organism: Homo sapiens
Primary publication:
A common allosteric site and mechanism in caspases.
Proc. Natl. Acad. Sci. U.S.A. 103 7595-600 (2006)
PMID: 16682620

Function and Biology Details

Reaction catalysed:
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|-.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Caspase-1 subunit p20 Chain: A
Molecule details ›
Chain: A
Length: 178 amino acids
Theoretical weight: 19.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P29466 (Residues: 120-297; Coverage: 44%)
Gene names: CASP1, IL1BC, IL1BCE
Structure domains: Rossmann fold
Caspase-1 subunit p10 Chain: B
Molecule details ›
Chain: B
Length: 88 amino acids
Theoretical weight: 10.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P29466 (Residues: 317-404; Coverage: 22%)
Gene names: CASP1, IL1BC, IL1BCE
Structure domains: Caspase-like
N-[(benzyloxy)carbonyl]-L-valyl-N-[(2S)-1-carboxy-4-fluoro-3-oxobutan-2-yl]-L-alaninamide Chain: C
Molecule details ›
Chain: C
Length: 5 amino acids
Theoretical weight: 472 Da

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P43212
Unit cell:
a: 63.006Å b: 63.006Å c: 161.279Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.214 0.272
Expression system: Escherichia coli